Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold
Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are transcriptionally upregulated in response to low temperature. Featuring an RNA-recognition motif (RRM) and an arginine–glycine-rich (RGG) domain, these prot...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 2016-10, Vol.73 (20), p.3839-3859 |
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| description | Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are transcriptionally upregulated in response to low temperature. Featuring an RNA-recognition motif (RRM) and an arginine–glycine-rich (RGG) domain, these proteins display many similarities and specific disparities in the regulation of numerous molecular and cellular events. The resistance to serum withdrawal, endoplasmic reticulum stress, or other harsh conditions conferred by RBM3 has led to its reputation as a survival gene. Once CIRP protein is released from cells, it appears to bolster inflammation, contributing to poor prognosis in septic patients. A variety of human tumor specimens have been analyzed for CIRP and RBM3 expression. Surprisingly, RBM3 expression was primarily found to be positively associated with the survival of chemotherapy-treated patients, while CIRP expression was inversely linked to patient survival. In this comprehensive review, we summarize the evolutionary conservation of CIRP and RBM3 across species as well as their molecular interactions, cellular functions, and roles in diverse physiological and pathological processes, including circadian rhythm, inflammation, neural plasticity, stem cell properties, and cancer development. |
| doi_str_mv | 10.1007/s00018-016-2253-7 |
| format | Article |
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Featuring an RNA-recognition motif (RRM) and an arginine–glycine-rich (RGG) domain, these proteins display many similarities and specific disparities in the regulation of numerous molecular and cellular events. The resistance to serum withdrawal, endoplasmic reticulum stress, or other harsh conditions conferred by RBM3 has led to its reputation as a survival gene. Once CIRP protein is released from cells, it appears to bolster inflammation, contributing to poor prognosis in septic patients. A variety of human tumor specimens have been analyzed for CIRP and RBM3 expression. Surprisingly, RBM3 expression was primarily found to be positively associated with the survival of chemotherapy-treated patients, while CIRP expression was inversely linked to patient survival. In this comprehensive review, we summarize the evolutionary conservation of CIRP and RBM3 across species as well as their molecular interactions, cellular functions, and roles in diverse physiological and pathological processes, including circadian rhythm, inflammation, neural plasticity, stem cell properties, and cancer development.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-016-2253-7</identifier><identifier>PMID: 27147467</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Amino Acid Sequence ; Animals ; Apoptosis ; Binding sites ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; blood serum ; carcinogenesis ; Cell Biology ; circadian rhythm ; cold ; Cold Temperature ; Disease ; endoplasmic reticulum ; Evolution, Molecular ; genes ; Humans ; inflammation ; Life Sciences ; Low temperature ; neoplasms ; Neurosciences ; patients ; prognosis ; Proteins ; Review ; Ribonucleic acid ; RNA ; RNA-binding proteins ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Stem cells ; Stress, Physiological - genetics ; temperature ; transcription (genetics)</subject><ispartof>Cellular and molecular life sciences : CMLS, 2016-10, Vol.73 (20), p.3839-3859</ispartof><rights>The Author(s) 2016</rights><rights>Springer International Publishing 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-918baea96fabd15c112cae1638b81bcbbafe77006e597b11dd54a3a7be05c93d3</citedby><cites>FETCH-LOGICAL-c536t-918baea96fabd15c112cae1638b81bcbbafe77006e597b11dd54a3a7be05c93d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5021741/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5021741/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,313,314,725,778,782,790,883,27905,27907,27908,41471,42540,51302,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27147467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhu, Xinzhou</creatorcontrib><creatorcontrib>Bührer, Christoph</creatorcontrib><creatorcontrib>Wellmann, Sven</creatorcontrib><title>Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are transcriptionally upregulated in response to low temperature. Featuring an RNA-recognition motif (RRM) and an arginine–glycine-rich (RGG) domain, these proteins display many similarities and specific disparities in the regulation of numerous molecular and cellular events. The resistance to serum withdrawal, endoplasmic reticulum stress, or other harsh conditions conferred by RBM3 has led to its reputation as a survival gene. Once CIRP protein is released from cells, it appears to bolster inflammation, contributing to poor prognosis in septic patients. A variety of human tumor specimens have been analyzed for CIRP and RBM3 expression. Surprisingly, RBM3 expression was primarily found to be positively associated with the survival of chemotherapy-treated patients, while CIRP expression was inversely linked to patient survival. In this comprehensive review, we summarize the evolutionary conservation of CIRP and RBM3 across species as well as their molecular interactions, cellular functions, and roles in diverse physiological and pathological processes, including circadian rhythm, inflammation, neural plasticity, stem cell properties, and cancer development.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>blood serum</subject><subject>carcinogenesis</subject><subject>Cell Biology</subject><subject>circadian rhythm</subject><subject>cold</subject><subject>Cold Temperature</subject><subject>Disease</subject><subject>endoplasmic reticulum</subject><subject>Evolution, Molecular</subject><subject>genes</subject><subject>Humans</subject><subject>inflammation</subject><subject>Life Sciences</subject><subject>Low temperature</subject><subject>neoplasms</subject><subject>Neurosciences</subject><subject>patients</subject><subject>prognosis</subject><subject>Proteins</subject><subject>Review</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA-binding proteins</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Stem cells</subject><subject>Stress, Physiological - genetics</subject><subject>temperature</subject><subject>transcription (genetics)</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkttrFDEYxYMo9qJ_gC8S8KUPHZsvM7nMi2AXL4WKUhTEl5DbdFNmkzWZqfS_N9tdSxVEnxL4fueE7-Qg9AzISyBEnBRCCMiGAG8oZW0jHqB96ChpeiLg4e7OJf26hw5Kuaowk5Q_RntUQCc6LvbRt0UaXROim20wo8frnCYfYsGLs4tPWEeHL04_tMdY4zmG77PHNs3ryv0I0xJrO4XrMAVf8KAzNv4mVcG03FCje4IeDXos_unuPERf3r75vHjfnH98d7Z4fd5Y1vKp6UEa7XXPB20cMAtArfbAW2kkGGuMHrwQhHDPemEAnGOdbrUwnjDbt649RK-2vuvZrLyzPk5Zj2qdw0rnG5V0UL9PYliqy3StGKEgOqgGRzuDnOqKZVKrUKwfRx19mouiNeZKCsr_iYKkQsr6Oew_UOh7QjlpK_riD_QqzTnW0G4pwgXAhoItZXMqJfvhbkUgatMHte2Dqn1Qmz4oUTXP72dzp_hVgArQLVDqKF76fO_pv7r-BOY_v3o</recordid><startdate>20161001</startdate><enddate>20161001</enddate><creator>Zhu, Xinzhou</creator><creator>Bührer, Christoph</creator><creator>Wellmann, Sven</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20161001</creationdate><title>Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold</title><author>Zhu, Xinzhou ; Bührer, Christoph ; Wellmann, Sven</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-918baea96fabd15c112cae1638b81bcbbafe77006e597b11dd54a3a7be05c93d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Binding sites</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>blood serum</topic><topic>carcinogenesis</topic><topic>Cell Biology</topic><topic>circadian rhythm</topic><topic>cold</topic><topic>Cold Temperature</topic><topic>Disease</topic><topic>endoplasmic reticulum</topic><topic>Evolution, Molecular</topic><topic>genes</topic><topic>Humans</topic><topic>inflammation</topic><topic>Life Sciences</topic><topic>Low temperature</topic><topic>neoplasms</topic><topic>Neurosciences</topic><topic>patients</topic><topic>prognosis</topic><topic>Proteins</topic><topic>Review</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA-binding proteins</topic><topic>RNA-Binding Proteins - 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Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular and molecular life sciences : CMLS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Xinzhou</au><au>Bührer, Christoph</au><au>Wellmann, Sven</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><stitle>Cell. Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2016-10-01</date><risdate>2016</risdate><volume>73</volume><issue>20</issue><spage>3839</spage><epage>3859</epage><pages>3839-3859</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are transcriptionally upregulated in response to low temperature. Featuring an RNA-recognition motif (RRM) and an arginine–glycine-rich (RGG) domain, these proteins display many similarities and specific disparities in the regulation of numerous molecular and cellular events. The resistance to serum withdrawal, endoplasmic reticulum stress, or other harsh conditions conferred by RBM3 has led to its reputation as a survival gene. Once CIRP protein is released from cells, it appears to bolster inflammation, contributing to poor prognosis in septic patients. A variety of human tumor specimens have been analyzed for CIRP and RBM3 expression. Surprisingly, RBM3 expression was primarily found to be positively associated with the survival of chemotherapy-treated patients, while CIRP expression was inversely linked to patient survival. In this comprehensive review, we summarize the evolutionary conservation of CIRP and RBM3 across species as well as their molecular interactions, cellular functions, and roles in diverse physiological and pathological processes, including circadian rhythm, inflammation, neural plasticity, stem cell properties, and cancer development.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>27147467</pmid><doi>10.1007/s00018-016-2253-7</doi><tpages>21</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Apoptosis Binding sites Biochemistry Biomedical and Life Sciences Biomedicine blood serum carcinogenesis Cell Biology circadian rhythm cold Cold Temperature Disease endoplasmic reticulum Evolution, Molecular genes Humans inflammation Life Sciences Low temperature neoplasms Neurosciences patients prognosis Proteins Review Ribonucleic acid RNA RNA-binding proteins RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Stem cells Stress, Physiological - genetics temperature transcription (genetics) |
| title | Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold |
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